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Database: UniProt
Entry: A0A1I6DYJ1_9RHOB
LinkDB: A0A1I6DYJ1_9RHOB
Original site: A0A1I6DYJ1_9RHOB 
ID   A0A1I6DYJ1_9RHOB        Unreviewed;       693 AA.
AC   A0A1I6DYJ1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   ORFNames=SAMN04515673_10685 {ECO:0000313|EMBL:SFR10569.1};
OS   Poseidonocella sedimentorum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Poseidonocella.
OX   NCBI_TaxID=871652 {ECO:0000313|EMBL:SFR10569.1, ECO:0000313|Proteomes:UP000199302};
RN   [1] {ECO:0000313|EMBL:SFR10569.1, ECO:0000313|Proteomes:UP000199302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC   {ECO:0000313|Proteomes:UP000199302};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00255};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
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DR   EMBL; FOYI01000006; SFR10569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6DYJ1; -.
DR   STRING; 871652.SAMN04515673_10685; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000199302; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   NCBIfam; TIGR00211; glyS; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00255};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00255};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00255}; Reference proteome {ECO:0000313|Proteomes:UP000199302}.
FT   DOMAIN          583..681
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   693 AA;  74520 MW;  CD9A6E5252FE8598 CRC64;
     MPDLLIELFS EEIPARMQRR ASEDLRKLMT DGLVEAGLTY RSAGAFATPR RLVLHIEDLL
     GASPTLREER KGPKVGAPEK AIEGFCRGAG VAIADLEARE TPKGAVYFAT VTTPGRPAAE
     IVADVLDKTI RNFPWPKSMR WGAGTLRWVR PLHSVLCILT DDAGEASVVP FEIEGIVAGN
     ETRGHRFMAP DAFSVGSFAD YTAKLKAAKV VLDPAERAEH IRADASNQAF AAGLEVVEDA
     GLLAEVAGLV EWPVVLVGEI GADFLDLPPE VLQTSMKEHQ KFFSLRDPKS GQITRFATVA
     NIETPDGGAT ILAGNQKVLS ARLSDAKFFW ENDLRTVERE GLQAMAAPLE NVTFHNKLGS
     QGARIARIAA LAEEIAPGVG ADPAQARLAA EIAKADLSSE MVYEFPELQG IMGRYYAMKA
     GLAQPVADAA RDHYAPLGPS DDVPVEPVSV AVALADKIDL LTGFWAIDEK PTGSKDPFAL
     RRAALGVIRI VLSNGLRLPL GAQFDAQLAR HEGAGEGLAA DLLGFVHDRL KVHLRDEGLR
     HDVIDACLEM EGGDDLASVV ARARALGAFV ETEEGTNLVQ GFRRANNILA QAEAKDGVEY
     SFGADAKYAE ADEERALFND LEAKGPEIAA AAKAERYGDA MAGMAALRAP IDAFFETVQI
     NAESEIVRRN RLNLLGQIRR ICGTVADLTR LEG
//
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